Current Protein Identity：A0A244EXR3
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 9YPI MboA HDO apo structure Deposited 2025-10-14 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
1–225（225 aa）
|
Not recorded | CL CHLORIDE ION × 5 SO4 SULFATE ION × 1 NA SODIUM ION × 2 GOL GLYCEROL × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method. Hanging drops were prepared by combining equal volumes of MboA (18 mg per mL) protein solution and reservoir solution (1.2 M lithium sulfate and 0.1 M sodium acetate, pH 4.6) for a total drop volume of 2 uL. Crystals typically grew in about approximately 1 to 2 weeks. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.49 Å R-free 0.221 |
| 9YPI MboA HDO apo structure Deposited 2025-10-14 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain B
1–225（225 aa）
|
Not recorded | CL CHLORIDE ION × 6 SO4 SULFATE ION × 1 NA SODIUM ION × 1 GOL GLYCEROL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method. Hanging drops were prepared by combining equal volumes of MboA (18 mg per mL) protein solution and reservoir solution (1.2 M lithium sulfate and 0.1 M sodium acetate, pH 4.6) for a total drop volume of 2 uL. Crystals typically grew in about approximately 1 to 2 weeks. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.49 Å R-free 0.221 |
| 9YPI MboA HDO apo structure Deposited 2025-10-14 | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain C
1–225（225 aa）
|
Not recorded | CL CHLORIDE ION × 5 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method. Hanging drops were prepared by combining equal volumes of MboA (18 mg per mL) protein solution and reservoir solution (1.2 M lithium sulfate and 0.1 M sodium acetate, pH 4.6) for a total drop volume of 2 uL. Crystals typically grew in about approximately 1 to 2 weeks. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.49 Å R-free 0.221 |
| 9YPI MboA HDO apo structure Deposited 2025-10-14 | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain D
1–225（225 aa）
|
Not recorded | CL CHLORIDE ION × 1 SO4 SULFATE ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method. Hanging drops were prepared by combining equal volumes of MboA (18 mg per mL) protein solution and reservoir solution (1.2 M lithium sulfate and 0.1 M sodium acetate, pH 4.6) for a total drop volume of 2 uL. Crystals typically grew in about approximately 1 to 2 weeks. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.49 Å R-free 0.221 |
| 9YPL MboA with Leu-Ala-Arg peptide substrate bound Deposited 2025-10-14 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
1–225（225 aa）
|
Not recorded | SO4 SULFATE ION × 2 CL CHLORIDE ION × 5 GOL GLYCEROL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.8；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method. Hanging drops were prepared by combining equal volumes of MboA (9 mg per mL) protein solution and reservoir solution (0.4 M lithium sulfate and 0.1 M sodium acetate, pH 4.8) for a total drop volume of 2 uL. The substrate bound structure was prepared by incubating apo crystals with 0.3 uL of 100 mM LAR in 0.1 M sodium acetate, pH 4.6 for two hours prior to looping. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.20 Å R-free 0.194 |
| 9YPL MboA with Leu-Ala-Arg peptide substrate bound Deposited 2025-10-14 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain B
1–225（225 aa）
|
Not recorded | SO4 SULFATE ION × 1 CL CHLORIDE ION × 4 GOL GLYCEROL × 1 ACT ACETATE ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.8；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method. Hanging drops were prepared by combining equal volumes of MboA (9 mg per mL) protein solution and reservoir solution (0.4 M lithium sulfate and 0.1 M sodium acetate, pH 4.8) for a total drop volume of 2 uL. The substrate bound structure was prepared by incubating apo crystals with 0.3 uL of 100 mM LAR in 0.1 M sodium acetate, pH 4.6 for two hours prior to looping. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.20 Å R-free 0.194 |
| 9YPL MboA with Leu-Ala-Arg peptide substrate bound Deposited 2025-10-14 | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain C
1–225（225 aa）
|
Not recorded | CL CHLORIDE ION × 3 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.8；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method. Hanging drops were prepared by combining equal volumes of MboA (9 mg per mL) protein solution and reservoir solution (0.4 M lithium sulfate and 0.1 M sodium acetate, pH 4.8) for a total drop volume of 2 uL. The substrate bound structure was prepared by incubating apo crystals with 0.3 uL of 100 mM LAR in 0.1 M sodium acetate, pH 4.6 for two hours prior to looping. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.20 Å R-free 0.194 |
| 9YPL MboA with Leu-Ala-Arg peptide substrate bound Deposited 2025-10-14 | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain D
1–225（225 aa）
|
Not recorded | SO4 SULFATE ION × 3 CL CHLORIDE ION × 2 GOL GLYCEROL × 1 ACT ACETATE ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.8；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method. Hanging drops were prepared by combining equal volumes of MboA (9 mg per mL) protein solution and reservoir solution (0.4 M lithium sulfate and 0.1 M sodium acetate, pH 4.8) for a total drop volume of 2 uL. The substrate bound structure was prepared by incubating apo crystals with 0.3 uL of 100 mM LAR in 0.1 M sodium acetate, pH 4.6 for two hours prior to looping. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.20 Å R-free 0.194 |
| 9YPM MboA with Leu-Ala-Arg peptide substrate and two Fe(II) ions bound Deposited 2025-10-14 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain A
1–225（225 aa）
|
Not recorded | SO4 SULFATE ION × 4 CL CHLORIDE ION × 4 FE2 FE (II) ION × 2 GOL GLYCEROL × 12 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method in an Coy anaerobic chamber with an atmosphere of < 5 ppm of O2. Hanging drops were prepared by combining equal volumes of MboA (9 mg/mL) protein solution, reservoir solution (0.6 M lithium sulfate and 0.1 M sodium acetate, pH 4.6), and 0.2 uL of a 1:1000 dilution microseed master stock generated from apo crystals for a total drop volume of 2.2 uL. The Fe(II) + substrate bound structure was prepared by incubating apo crystals with 0.4 uL of 100 mM LAR peptide and 100 mM Fe2+ in 0.1 M sodium acetate, pH 4.6 for two hours prior to looping. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.45 Å R-free 0.195 |
| 9YPM MboA with Leu-Ala-Arg peptide substrate and two Fe(II) ions bound Deposited 2025-10-14 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain B
1–225（225 aa）
|
Not recorded | SO4 SULFATE ION × 5 CL CHLORIDE ION × 4 FE2 FE (II) ION × 2 GOL GLYCEROL × 7 ACT ACETATE ION × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method in an Coy anaerobic chamber with an atmosphere of < 5 ppm of O2. Hanging drops were prepared by combining equal volumes of MboA (9 mg/mL) protein solution, reservoir solution (0.6 M lithium sulfate and 0.1 M sodium acetate, pH 4.6), and 0.2 uL of a 1:1000 dilution microseed master stock generated from apo crystals for a total drop volume of 2.2 uL. The Fe(II) + substrate bound structure was prepared by incubating apo crystals with 0.4 uL of 100 mM LAR peptide and 100 mM Fe2+ in 0.1 M sodium acetate, pH 4.6 for two hours prior to looping. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.45 Å R-free 0.195 |
| 9YPM MboA with Leu-Ala-Arg peptide substrate and two Fe(II) ions bound Deposited 2025-10-14 | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain C
1–225（225 aa）
|
Not recorded | SO4 SULFATE ION × 3 CL CHLORIDE ION × 2 FE2 FE (II) ION × 2 GOL GLYCEROL × 10 ACT ACETATE ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method in an Coy anaerobic chamber with an atmosphere of < 5 ppm of O2. Hanging drops were prepared by combining equal volumes of MboA (9 mg/mL) protein solution, reservoir solution (0.6 M lithium sulfate and 0.1 M sodium acetate, pH 4.6), and 0.2 uL of a 1:1000 dilution microseed master stock generated from apo crystals for a total drop volume of 2.2 uL. The Fe(II) + substrate bound structure was prepared by incubating apo crystals with 0.4 uL of 100 mM LAR peptide and 100 mM Fe2+ in 0.1 M sodium acetate, pH 4.6 for two hours prior to looping. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.45 Å R-free 0.195 |
| 9YPM MboA with Leu-Ala-Arg peptide substrate and two Fe(II) ions bound Deposited 2025-10-14 | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
Chain D
1–225（225 aa）
|
Not recorded | SO4 SULFATE ION × 3 CL CHLORIDE ION × 2 FE2 FE (II) ION × 2 GOL GLYCEROL × 7 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；MboA crystals were prepared via the hanging drop vapor diffusion method in an Coy anaerobic chamber with an atmosphere of < 5 ppm of O2. Hanging drops were prepared by combining equal volumes of MboA (9 mg/mL) protein solution, reservoir solution (0.6 M lithium sulfate and 0.1 M sodium acetate, pH 4.6), and 0.2 uL of a 1:1000 dilution microseed master stock generated from apo crystals for a total drop volume of 2.2 uL. The Fe(II) + substrate bound structure was prepared by incubating apo crystals with 0.4 uL of 100 mM LAR peptide and 100 mM Fe2+ in 0.1 M sodium acetate, pH 4.6 for two hours prior to looping. Crystals were cryoprotected with the addition of 0.75 uL of 40% glycerol in 0.1 M sodium acetate, pH 4.6 and flash frozen in LN2
|
Resolution 2.45 Å R-free 0.195 |